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- PDB-9hho: A conserved beta-sandwich fold is required for secretion of lipop... -

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Basic information

Entry
Database: PDB / ID: 9hho
TitleA conserved beta-sandwich fold is required for secretion of lipoproteins by a novel Type I secretion system
ComponentsProtein CexE
KeywordsTRANSPORT PROTEIN / Type I secretion CexE Aat system bacterial secretion
Function / homology: / periplasmic space / Protein CexE
Function and homology information
Biological speciesEscherichia coli ETEC H10407 (bacteria)
MethodSOLUTION NMR / simulated annealing
AuthorsHodges, F.J. / Icke, C. / Knowles, T.J. / Rooke, J.L. / Cole, J.A. / Cunningham, A.F. / Torres, V.V.L. / Henderson, I.R.
Funding support Australia, 1items
OrganizationGrant numberCountry
Australian Research Council (ARC)GA68330-V2 Australia
CitationJournal: To Be Published
Title: A conserved beta-sandwich fold is required for secretion of lipoproteins by a novel Type I secretion system
Authors: Hodges, F.J. / Icke, C. / Knowles, T.J. / Rooke, J.L. / Cole, J.A. / Cunningham, A.F. / Torres, V.V.L. / Henderson, I.R.
History
DepositionNov 22, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 3, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Protein CexE


Theoretical massNumber of molelcules
Total (without water)11,7641
Polymers11,7641
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: NMR Distance Restraints, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 60structures with acceptable covalent geometry
RepresentativeModel #1lowest energy

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Components

#1: Protein Protein CexE / CfaD-dependent expression extracytoplasmic protein


Mass: 11764.057 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli ETEC H10407 (bacteria)
Gene: cexE / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A2TJI4
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic22D 1H-15N HSQC
121isotropic13D HNCA
131isotropic13D HN(CO)CA
141isotropic13D HN(CA)CB
151isotropic13D HN(COCA)CB
161isotropic13D HNCO
171isotropic13D HN(CA)CO
181isotropic13D H(CCO)NH
191isotropic13D H(CCO)NH
1101isotropic23D 1H-13C NOESY
1111isotropic23D 1H-15N NOESY

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Sample preparation

DetailsType: solution
Contents: 1.83 mM [U-100% 13C; U-100% 15N] CexE, 20 mM sodium phosphate, 150 mM sodium chloride, 50 mM L-glutamine, 50 mM L-arginine, 0.5 mM TCEP, 90% H2O/10% D2O
Label: 15N13C_sample / Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1.83 mMCexE[U-100% 13C; U-100% 15N]1
20 mMsodium phosphatenatural abundance1
150 mMsodium chloridenatural abundance1
50 mML-glutaminenatural abundance1
50 mML-argininenatural abundance1
0.5 mMTCEPnatural abundance1
Sample conditionsIonic strength: 150 mM / Label: Conditions_1 / pH: 6.5 / Pressure: 1 bar / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCE IIIBrukerAVANCE III6001
Bruker AVANCE IIIBrukerAVANCE III9002

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Processing

NMR software
NameDeveloperClassification
SparkyGoddardchemical shift assignment
CYANAGuntert, Mumenthaler and Wuthrichstructure calculation
ARIALinge, O'Donoghue and Nilgesrefinement
SparkyGoddardpeak picking
RefinementMethod: simulated annealing / Software ordinal: 3
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with acceptable covalent geometry
Conformers calculated total number: 60 / Conformers submitted total number: 20

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